Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aldose reductase

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Alditol + NAD(P)+ = aldose + NAD(P)H.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei60Proton donorBy similarity1
Sitei88Lowers pKa of active site TyrBy similarity1
Binding sitei121SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi215 – 269NADPBy similarityAdd BLAST55

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose reductase (EC:1.1.1.21)
Short name:
AR
Alternative name(s):
Aldehyde reductase
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001246281 – 320Aldose reductaseAdd BLAST320

Expressioni

Inductioni

By abscisic acid (ABA) and gibberellic acid (GA).

Interactioni

Protein-protein interaction databases

STRINGi4513.MLOC_54711.3.

Structurei

Secondary structure

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 17Combined sources3
Beta strandi23 – 27Combined sources5
Helixi35 – 37Combined sources3
Helixi38 – 47Combined sources10
Beta strandi53 – 55Combined sources3
Helixi58 – 60Combined sources3
Helixi63 – 75Combined sources13
Helixi80 – 82Combined sources3
Beta strandi84 – 89Combined sources6
Helixi91 – 93Combined sources3
Helixi96 – 98Combined sources3
Helixi99 – 110Combined sources12
Beta strandi115 – 123Combined sources9
Helixi144 – 156Combined sources13
Beta strandi159 – 167Combined sources9
Helixi170 – 179Combined sources10
Beta strandi185 – 190Combined sources6
Helixi198 – 206Combined sources9
Beta strandi210 – 215Combined sources6
Turni219 – 222Combined sources4
Helixi224 – 226Combined sources3
Helixi228 – 237Combined sources10
Helixi241 – 252Combined sources12
Beta strandi255 – 257Combined sources3
Helixi263 – 268Combined sources6
Helixi279 – 287Combined sources9
Helixi298 – 301Combined sources4
Turni304 – 306Combined sources3
Helixi312 – 315Combined sources4
Turni316 – 318Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BGQX-ray2.50A2-320[»]
2BGSX-ray1.64A2-320[»]
2VDGX-ray1.92A2-320[»]
ProteinModelPortaliP23901.
SMRiP23901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23901.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAKATMGQ GEQDHFVLKS GHAMPAVGLG TWRAGSDTAH SVRTAITEAG
60 70 80 90 100
YRHVDTAAEY GVEKEVGKGL KAAMEAGIDR KDLFVTSKIW CTNLAPERVR
110 120 130 140 150
PALENTLKDL QLDYIDLYHI HWPFRLKDGA HMPPEAGEVL EFDMEGVWKE
160 170 180 190 200
MENLVKDGLV KDIGVCNYTV TKLNRLLRSA KIPPAVCQME MHPGWKNDKI
210 220 230 240 250
FEACKKHGIH VTAYSPLGSS EKNLAHDPVV EKVANKLNKT PGQVLIKWAL
260 270 280 290 300
QRGTSVIPKS SKDERIKENI QVFGWEIPEE DFKVLCSIKD EKRVLTGEEL
310 320
FVNKTHGPYR SAADVWDHEN
Length:320
Mass (Da):35,807
Last modified:November 1, 1991 - v1
Checksum:i5AA72C021E9A93C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57526 Genomic DNA. Translation: CAA40747.1.
PIRiS15024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57526 Genomic DNA. Translation: CAA40747.1.
PIRiS15024.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BGQX-ray2.50A2-320[»]
2BGSX-ray1.64A2-320[»]
2VDGX-ray1.92A2-320[»]
ProteinModelPortaliP23901.
SMRiP23901.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4513.MLOC_54711.3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.

Miscellaneous databases

EvolutionaryTraceiP23901.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALDR_HORVU
AccessioniPrimary (citable) accession number: P23901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.